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Protease inhibitors in bacteria: an emerging concept for the regulation of bacterial protein complexes?
Author(s) -
Schwarz Wolfgang H.,
Zverlov Vladimir V.
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05181.x
Subject(s) - biology , proteases , protease , serpin , serine protease , biochemistry , microbiology and biotechnology , bacteria , serine , tmprss6 , masp1 , enzyme , gene , genetics
Summary Serine protease inhibitors (serpins), the antagonists of serine proteases, were unknown in the bacterial kingdom until recently. Kang et al . in this issue of Molecular Microbiology report the cloning and functional analysis of the three serpin genes from the thermophilic anaerobic bacterium Clostridium thermocellum . Two of the serpins contain a dockerin module for location in the extracellular hydrolytic multienzyme complex, the cellulosome. The susceptibility of cellulosome to proteolytic degradation and the presence of a serine protease in the same complex provoke speculation that protease inhibitor/protease pairs could play hitherto unrecognized roles in protein stability and regulation in bacteria.

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